Zinc in PDB 2mpj: uc(Nmr) Structure of Xenopus RECQ4 Zinc Knuckle

The binding sites of Zinc atom in the uc(Nmr) Structure of Xenopus RECQ4 Zinc Knuckle (pdb code 2mpj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the uc(Nmr) Structure of Xenopus RECQ4 Zinc Knuckle, PDB code: 2mpj:

Zinc binding site 1 out of 1 in the uc(Nmr) Structure of Xenopus RECQ4 Zinc Knuckle


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of Xenopus RECQ4 Zinc Knuckle within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:0.2 occ:1.00 NE2 A:HIS15 2.0 0.1 1.0 SG A:CYS7 2.3 0.2 1.0 SG A:CYS20 2.3 0.3 1.0 SG A:CYS10 2.3 0.2 1.0 CE1 A:HIS15 2.5 0.1 1.0 HE1 A:HIS15 2.7 0.2 1.0 CD2 A:HIS15 2.9 0.1 1.0 HB3 A:CYS7 3.1 0.1 1.0 HB3 A:CYS10 3.1 0.3 1.0 HA A:CYS20 3.2 0.3 1.0 CB A:CYS7 3.3 0.2 1.0 CB A:CYS10 3.4 0.2 1.0 CB A:CYS20 3.4 0.5 1.0 HD2 A:HIS15 3.4 0.1 1.0 H A:CYS10 3.4 0.6 1.0 HA A:ALA17 3.5 0.6 1.0 ND1 A:HIS15 3.5 0.1 1.0 HB3 A:CYS20 3.5 0.9 1.0 CG A:HIS15 3.7 0.1 1.0 CA A:CYS20 3.7 0.3 1.0 HB2 A:CYS7 3.8 0.3 1.0 N A:CYS10 4.1 0.2 1.0 HB2 A:CYS10 4.1 0.3 1.0 N A:CYS20 4.1 0.3 1.0 HD2 A:PRO21 4.2 0.7 1.0 O A:TRP16 4.3 0.2 1.0 H A:CYS20 4.3 0.3 1.0 HD1 A:HIS15 4.3 0.2 1.0 HB2 A:CYS20 4.3 0.8 1.0 CA A:CYS10 4.3 0.2 1.0 HB2 A:ARG9 4.4 0.5 1.0 H A:GLY12 4.4 0.2 1.0 CA A:ALA17 4.5 0.4 1.0 CA A:CYS7 4.6 0.2 1.0 HB3 A:ARG9 4.6 0.5 1.0 O A:CYS7 4.7 0.2 1.0 O A:ALA17 4.7 0.6 1.0 H A:ARG9 4.7 0.2 1.0 C A:TRP16 4.7 0.2 1.0 O A:HIS15 4.8 0.2 1.0 C A:GLN19 4.9 0.2 1.0 N A:ALA17 4.9 0.3 1.0 C A:CYS7 4.9 0.2 1.0 H A:GLY11 4.9 0.1 1.0 C A:ALA17 4.9 0.4 1.0 HA A:CYS7 4.9 0.2 1.0 HD3 A:PRO21 4.9 0.6 1.0 H A:GLN19 4.9 0.3 1.0 CB A:ARG9 5.0 0.3 1.0

F.Marino, A.Mojumdar, C.Zucchelli, A.Bhardwaj, E.Buratti, A.Vindigni, G.Musco, S.Onesti. Structural and Biochemical Characterization of An Rna/Dna Binding Motif in the N-Terminal Domain of RECQ4 Helicases Sci Rep V. 6 21501 2016.
ISSN: ESSN 2045-2322
PubMed: 26888063
DOI: 10.1038/SREP21501